Reference : Staphylolytic Enzyme from Chalaropsis: Mechanism of Action

	Document type :	Scientific journals : Article
	Discipline(s) :	Human health sciences : Pharmacy, pharmacology & toxicology Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/93328

Title :	Staphylolytic Enzyme from Chalaropsis: Mechanism of Action
Language :	English
Author, co-author :	Tipper, Donald J. [University of Wisconsin > Medicale School - Department of Pharmacology > > >]
	Strominger, Jack L. [University of Wisconsin > Medicale School - Department of Pharmacology > > >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > > > Service de Bactériologie > > >]
Publication date :	6-Nov-1964
Journal title :	Science
Publisher :	American Association for the Advancement of Science
Volume :	146
Pages :	781-782
Audience :	International
ISSN :	0036-8075
e-ISSN :	1095-9203
City :	Washington
Country :	DC
Keywords :	[en] glycoside hydrolases ; pharmacology ; research ; staphylococcus
Abstract :	[en] The staphylolytic enzyme recently isolated from cultures of a Chalaropsis species by Hash is shown to be an acetylmurainidase that cleaves all the glycosidic linkages of N-acetylmuramic acid and N,O-diacetylmuramic acid in the cell wall of Staphylococcus aureus strain Copenhagen. It is similar in specificity to the "32 enzyme" from Streptomyces albus but it differs from egg-white lysozyme whose activity is inhibited by the presence of O-acetyl groups.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/93328

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